Data extracted from this reference:

Cloned(Commentary)

Commentary

Organism

the sequence motif is introduced into a mesophilic Escherichia coli isopropylmalate dehydrogenase, one by one. The introduction of the whole motif leads the mesophilic enzyme to be more unstable whereas substitution of only one amino acid residue in the motif thermostabilizes the enzyme

mutant enzyme L204F shows higher thermostability compared to wild-type enzyme, denaturation rates at 68°C and 70°C are slower for the mutant enzyme than for wild-type enzyme

Thermus thermophilus

87

-

the thermophilic IMPDH was succesfully stabilized by replacing Ala172 with more hydrophobic residues like Glu, Asn and Gln without significant change in the enzymatic activity

Thermus thermophilus

Cofactor

Cofactor

Commentary

Organism

Structure

NAD+

-

Escherichia coli

NAD+

-

Thermus thermophilus

Cloned(Commentary) (protein specific)

Commentary

Organism

the sequence motif is introduced into a mesophilic Escherichia coli isopropylmalate dehydrogenase, one by one. The introduction of the whole motif leads the mesophilic enzyme to be more unstable whereas substitution of only one amino acid residue in the motif thermostabilizes the enzyme